2vf9 | pdb_00002vf9

Crystal structure of bacteriophage PRR1

spinqualitylabelsall models 2vf9, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vf9 is a 3 chain structure with sequence from Bpprr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [COAT_BPPRR] Forms the phage shell; binds to the phage RNA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Many nonenveloped virus particles are stabilized by calcium ions bound in the interfaces between the protein subunits. These ions may have a role in the disassembly process. The small RNA phages of the Leviviridae family have T=3 quasi-symmetry and are unique among simple viruses in that they have a coat protein with a translational repressor activity and a fold that has not been observed in other viruses. The crystal structure of phage PRR1 has been determined to 3.5 A resolution. The structure shows a tentative binding site for a calcium ion close to the quasi-3-fold axis. The RNA-binding surface used for repressor activity is mostly conserved. The structure does not show any significant differences between quasi-equivalent subunits, which suggests that the assembly is not controlled by conformational switches as in many other simple viruses. The capsid of the small RNA phage PRR1 is stabilized by metal ions.,Persson M, Tars K, Liljas L J Mol Biol. 2008 Nov 21;383(4):914-22. Epub 2008 Aug 29. PMID:18786545 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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